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The catalytic efficiency of METTL16 affects cellular methyltransferase activities by governing the intracellular S-adenosylmethionine setpoint

ABSTRACT: The catalytic efficiency of METTL16 affects cellular methyltransferase activities by governing the intracellular S-adenosylmethionine setpoint

PROVIDER: PRJNA1258953 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR33440421_1.fastq.gz	Fastqsanger.gz
	SRR33440421_2.fastq.gz	Fastqsanger.gz
	SRR33440422_1.fastq.gz	Fastqsanger.gz
	SRR33440422_2.fastq.gz	Fastqsanger.gz
	SRR33440423_1.fastq.gz	Fastqsanger.gz

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The catalytic efficiency of METTL16 affects cellular methyltransferase activities by governing the intracellular S-adenosylmethionine setpoint

Project description:S-adenosylmethionine (SAM) regulates multiple cell processes as the methyl donor for cellular methyltransferases. The N6-methyladenosine (m6A) methyltransferase METTL16 regulates the expression of the SAM synthetase MAT2A, but it has been unclear if this regulation supports SAM homeostasis in a physiologically relevant way. Here, we used a degron and complementation strategy in HCT116 cells to demonstrate that disruption of MAT2A regulation by METTL16 has consequences for a wide variety of SAM-dependent processes including histone methylation, translation, m6A and m6Am RNA methylation. We also identified several U6 snRNA psuedogenes, including those with non-canonical consensus motifs, that are methylated by METTL16. Complementation by a catalytically hyperactive METTL16 abrogates MAT2A regulation and decreases intracellular SAM concentrations. Moreover, these complemented cells are hypersensitive to treatment with a MAT2A inhibitor and to deletion of the MTAP gene, which is lost in nearly 15% of all cancers. These findings support the conclusion that the catalytic efficiency of METTL16 helps establish the SAM setpoint in cells and that this function could be exploited as a potential treatment for MTAP-deficient cancers.

2025-06-03 | GSE296342 | GEO

Determine the methyltransferase activities of METTL16 via MeRIP-seq (m6A-seq)

Project description:METTL16 belongs to methyltransferase like (METTL) family and could install m6A marks on its substrates. Here, we uncover a tumor-promoting role of METTL16 in AML and LSC self-renewal. To explore the mechanism underlying the oncogenic function of METTL16 in AML, we performed m6A-seq and RNA-seq. Via integrated analysis of m6A-seq data and RNA-seq data, we identified two bona fide targets of METTL16, BCAT1 and BCAT2. METTL16 functions as an m6A methyltransferase to regulate expression of BCAT1 and BCAT2, which contribute to reprogramming of BCAA metabolism.

2023-01-12 | GSE189995 | GEO

The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention

Project description:Maintenance of the intracellular levels of the methyl donor S-adenosylmethionine (SAM) is essential for a wide variety of biological processes. We demonstrate that the N6-adenosine methyltransferase METTL16 regulates expression of MAT2A, which encodes the only SAM synthetase expressed in most cells. Upon SAM depletion by methionine starvation, cells induce MAT2A expression by enhanced splicing of a retained intron. Induction requires METTL16 and its methylation substrate, a vertebrate conserved hairpin (hp1) in the MAT2A 3´ UTR. Increasing METTL16 occupancy on the MAT2A 3´ UTR is sufficient to induce efficient splicing. We propose that under SAM-limiting conditions, METTL16 occupancy on hp1 increases due to inefficient enzymatic turnover, which in turn promotes MAT2A splicing. Interestingly, human and S. pombe METTL16 methylate the U6 spliceosomal snRNA at a sequence identical to hp1. These observations suggest that the conserved U6 snRNA methyltransferase evolved an additional function in vertebrates to regulate SAM homeostasis.

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RNA-seq in wild-type, METTL16-knockout, and METTL16 rescue NOMO-1 cells

2023-01-12 | GSE190044 | GEO

Determine the methyltransferase activities of METTL3, METTL14, and METTL16 via MeRIP-seq (m6A-seq)

Project description:All the three enzymes, METTL3, METTL14, and METTL16, belong to methyltransferase like (METTL) family and possess the ability to deposit N6-methyladenosine (m6A) in mRNA. Via immunofluorescence staining and wertern blotting, we discovered either METTL3 or METTL14 mainly localize in nuclear, but METTL16 localizes in both cytosol and nuclei. To compare the m6A methyltransferase activities of the three m6A 'writers' and better understand their differences, MeRIP-seq (m6A-seq) was conducted with poly(A) RNAs isolaed from HEK293T cells with METTL3, 14 and 16 knockout.

2021-10-28 | GSE182607 | GEO

METTL16 promotes translation and lung tumorigenesis by sequestering cytoplasmic eIF4E2

Project description:METTL16 was previously identified as an m6A methyltransferase. In this study, we validated the cytoplasmic location of METTL16 and explored its function in the cytoplasm. We found that METTL16 promoted translation by sequestering eIF4E2, a translation initiation repressor, from the 5' cap structure.

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Identifying interaction proteins of METTL16 using co immunoprecipitation and mass spectroscopy

Project description:METTL16 has recently been identified as an RNA methyltransferase that installs m6A marks on a few transcripts. But its function in cytosol remains unclear. Puromycin-labelling and renilla luciferase assay revealed that METTL16 can promote translation efficiency in an m6A-independent manner. To explore the mechanism, we performed co-immunoprecipitation using METTL16 antibody and mass spectroscopy to identify its interaction proteins. Moreover, we find that METTL16 is essential for tumorigenesis of non-small cell lung cancer.

2024-08-03 | PXD032068 | Pride

RNA Methyltransferase METTL16's Protein Domains Have Differential Functional Effects on Cell Processes

Project description:To investigate the cellular role of METTL16, we established HEK293 cell lines over expressing wild-type METTL16 or METTL16 methylation and RNA binding mutations. We then removed endogenous METTL16 from the cells using CRISPR. We then performed gene expression profiling analysis using data obtained from RNA-seq of the various cell lines.

2023-06-29 | GSE217192 | GEO

Determine the effects of METTL16 on global translation efficiency via ribosome profiling (Ribo-seq)

Project description:METTL16 is a member of methyltransferase like (METTL) family. Unlike well-studied METTL3 and METTL14, we found a much higher percentage of METTL16 is localized in the cytosol. The subcellular distribution holds the ability to potentiate translation efficiency. Via Far-western blotting and Co-Immunoprecipitation (Co-IP) assays, we have identified the direct interactions between METTL16 and eukaryotic initiation factor 3 (eIF3) a and b. Via cross-linking immunoprecipitation and qPCR (CLIP-qPCR), we have discovered the direct associations between METTL16 and rRNAs. The METTL16-eIF3a/b and METTL16-rRNAs interactions induce the binding between eIF3 and 18S rRNA, promote the formation of 43S preinitiation complex, and eventually expedite translation initiation, the rate-limiting step of translation. To determine the exact effects of METTL16 on translation efficiency, we performed ribosome profiling (Ribo-seq) with HEK293T upon CRISPR-Cas9-induced METTL16 knockout. To guarantee the repeatability and avoid any potential off-target effects, we included 3 distint sgRNAs against METTL16.

2021-10-28 | GSE156796 | GEO

Determining the methyltransferase activities of METTL3, METTL14, and METTL16

Project description:Determining the methyltransferase activities of METTL3, METTL14, and METTL16

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